McDonald T L, Mallavia L
J Bacteriol. 1971 Sep;107(3):864-9. doi: 10.1128/jb.107.3.864-869.1971.
Purified preparations of Coxiella burnetii were examined for enzymes of the glycolytic pathway. Glucose-phosphate isomerase, fructose-1,6-diphosphatase, aldolase, glyceraldehyde-3-phosphate dehydrogenase, and pyruvate kinase were shown to be present in C. burnetii extracts. Heat-killed C. burnetii purified with normal yolk sacs demonstrated no activity after disruption. Aldolase was shown to be of the class II type by complete inhibition of activity in the presence of 8 x 10(-3)m ethylenediaminetetraacetic acid. The host enzyme activity (normal and infected yolk sacs) was not affected by the same treatment. When cellulose acetate electrophoresis was performed on the extracts, aldolase from both normal and infected yolk sacs exhibited five isozyme bands, whereas aldolase from the C. burnetii extract appeared as a single band.
对纯化的伯氏考克斯氏体制剂进行了糖酵解途径酶的检测。结果显示,葡萄糖 - 磷酸异构酶、果糖 - 1,6 - 二磷酸酶、醛缩酶、甘油醛 - 3 - 磷酸脱氢酶和丙酮酸激酶存在于伯氏考克斯氏体提取物中。用正常卵黄囊纯化的热灭活伯氏考克斯氏体在破碎后无活性。在存在8×10⁻³m乙二胺四乙酸的情况下,醛缩酶活性完全被抑制,表明其为II类。相同处理对宿主酶活性(正常和感染的卵黄囊)没有影响。当对提取物进行醋酸纤维素电泳时,正常和感染卵黄囊的醛缩酶均呈现五条同工酶带,而伯氏考克斯氏体提取物中的醛缩酶呈现为一条带。